COOCOOC-NH2CH2CH213CH2CH2CH24CH2H--NH3-NH3H-CCOOCO-АCa. Aminotransferase is the only enzyme that can catalyze theB -> C conversionb. Reaction 4 requires ATPc. All reactions (1-4) run only in the liverd. Compound A is a nitrogen donor for synthesis of 5-ribosylaminee. Reaction 1 is a hydrolysis and the enzyme catalyzing thisreaction is active only in hepatocytes

Ans). A) Glutamine B) Glutamate C) α-Ketoglutarate

Answered: COO COO C -NH2 CH2 CH2 1 3 CH2 CH2 CH2…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?
Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
Can u help me to explain to me, please? I stuggled. I don't understand The a-ketoglutarate that is produced inthe reaction is now free to accept a new quaternary ammonium group from another amino acid in a transamination reaction.
Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
Pepsin, a peptidase that hydrolyzes proteins, functions in the stomach at an optimum pH of 1.5–2.0. How is the rate of a pepsin-catalyzed reaction affected by each of thefollowing conditions? increasing the concentration ofproteins changing the pH to0 running the reaction at 0°C using lesspepsin
if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
A(n) _________ reaction converts glycylalanine to glycine and alanine. This reaction requires __________. Blank 1 options- Oxidation-reduction Hydrolysis Isomerization Group transfer Internal rearrangement Blank 2 options- H2O and apeptidase or a protease H2O and a phosphatase ADP and a phosphatase NAD+ and a peptidase or a protease
Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral intermediate collapses and product 2 released. -Aromatic R group of polypeptide substrate is positioned in hydrophobic pocket and the carbonyl of that residue is positioned in the oxyanion hole -His57 deprotonates Ser195 -Formation of acyl-enzyme intermediate -Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195. -Tetrahedra intermediate collapses and product 1 released -H2O enters active site of chumotrunsir -Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole -His57 deprotonates H20 -H20 does nucleophilic attack on carbonyl of substrate in oxyanion hole
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
Based on this information, what type of enzyme would ornithine decarboxylase be? I searched it up on Google and sources say it is a lyase because it catalyzes cleavage without H2O, but in equation 1, isn't water part of the reaction? Is decarboxylase still a lyase because water is a reactant, not a catalyst?
for the following reactions: arrive at the Michaelis menten enzyme kinetics: E+2A <-----k1,k2----->A.E+A reversible A.E+A<------k3,k4------>A 2E reversible A2.E------k5--------> E+CD non-reverisble show all steps

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